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+ | |||
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− | + | <h2 id="caption">OFF to pri<span class="swapper0">ON</span></h2><br> | |
− | + | <h4 id="title">Using stop codon read-through and CRISPR to explore <i>S. cerevisiae</i> prion mechanisms </h1> | |
− | + | ||
− | + | </div> | |
− | + | ||
− | + | </div> | |
− | + | ||
− | |||
− | |||
− | + | <div class="col-xs-2 changing-circles hidden-sm hidden-xs "> | |
− | + | <div id="circle4" class="swapper2"></div><br> | |
− | + | <div id="circle5" class="swapper3"></div><br> | |
− | + | <div id="circle6" class="swapper1"></div><br> | |
− | + | <div id="circle4" class="swapper2"></div><br> | |
− | + | <div id="circle5" class="swapper3"></div><br> | |
− | + | <div id="circle6" class="swapper1"></div><br> | |
− | + | </div> | |
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− | / | + | |
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− | + | </div> | |
− | + | </div> | |
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− | + | <br> | |
− | + | <div class="yeastpan"> | |
− | + | <div class="overlay"></div> | |
− | + | <h3 class="pan-text"> <span class="pan-background">Furthering the advancement of research into prions and neurodegenerative diseases | |
+ | </span></h3> | ||
+ | </div> | ||
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− | + | <div class="container-fluid tsc"> | |
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− | + | <div class="col-md-4 center"><img class="tsc1" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/0/01/T--Waterloo--Trigger_landing.png" > | |
− | + | <h4 id="texticles1"> We initiate a [PSI+] response in S. cerevisiae using a plasmid that will overexpress Sup35-NM. </h4></div> | |
− | + | <div class="col-md-4 center"><img class="tsc2" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/e/e0/T--Waterloo--Signal_landing.png"> | |
− | + | <h4 id="texticles2"> We insert a premature stop codon into an N-terminal CFP tag that will be read through and fluoresce during a [PSI+] response</h4></div> | |
− | + | <div class="col-md-4 center"><img class="tsc3" style="width: 15vw" src="https://static.igem.org/mediawiki/2016/f/fe/T--Waterloo--Control_landing.png" > | |
− | + | <h4 id="texticles3">We control read through rates by choosing the location of the premature stop codon, and can therefore control protein production in [PSI+]. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. </h4> </div> | |
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− | + | </div> | |
− | + | <div style="background: rgba(30,144,255, 0.4)"> | |
− | + | <div class="pan-text"><span style="color: #F6536D">ABSTRACT</span> </div> | |
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− | + | <h3 style="text-shadow: 2px 2px #999999; padding:0vw 10vw 10vh 10vw"> | |
− | + | Prions, or “zombie proteins,” are infectious agents that lead to a variety of neurodegenerative disorders (NDDs). They sicken cells by aggregating with each other and prevent proper protein folding leading to cell death from the accumulated damage. We propose a synthetic biology approach to better study prion propagation in the model organism S. cerevisiae. Our system involves inserting a premature stop codon into a protein open reading frame of interest or into dCas9 to respectively overexpress or knock-down protein levels during a [PSI+] response. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. This research is useful for continuously observing a phenotypic output during prion propagation in yeast and may have implications for helping to identify protein targets for both prevention and treatment of NDDs in the future. | |
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− | . | + | <script> |
− | + | $(document).ready(function(){ | |
− | + | function toprion(){ | |
− | + | $(".swapper1") | |
− | + | .animate({'background-color':'#fdf9d2', svgFill:'#ffe86a'}, 1500) | |
− | + | .animate({'background-color':'#F5C2C7', svgFill: '#F5C2C7'},500) | |
− | } | + | .animate({'background-color':'#F5636D', svgFill: '#F5636D'},1500, toprion); |
+ | }; | ||
+ | function toprion2(){ | ||
+ | $(".swapper2") | ||
+ | .animate({'background-color':'#fdf9d2'}, 1800) | ||
+ | .animate({'background-color':'#F5C2C7'},1200) | ||
+ | .animate({'background-color':'#F5636D'},500, | ||
+ | toprion2) | ||
+ | }; | ||
+ | function toprion3(){ | ||
+ | $(".swapper3") | ||
+ | .animate({'background-color':'#fdf9d2'}, 1000) | ||
+ | .animate({'background-color':'#F5C2C7'},1200) | ||
+ | .animate({'background-color':'#F5636D'},2000, | ||
+ | toprion3) | ||
+ | }; | ||
+ | toprion3(); | ||
+ | toprion2(); | ||
+ | toprion(); | ||
− | . | + | $("#texticles1").hide() |
− | + | $("#texticles2").hide() | |
− | } | + | $("#texticles3").hide() |
+ | $(".tsc1").on("click", function(){ | ||
+ | $("#texticles1").slideToggle() | ||
+ | }) | ||
+ | $(".tsc2").on("click", function(){ | ||
+ | $("#texticles2").slideToggle() | ||
+ | }) | ||
+ | $(".tsc3").on("click", function(){ | ||
+ | $("#texticles3").slideToggle() | ||
+ | }) | ||
+ | }) | ||
+ | </script> | ||
+ | </body> | ||
+ | </html> | ||
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Latest revision as of 23:59, 19 October 2016
OFF to priON
Using stop codon read-through and CRISPR to explore S. cerevisiae prion mechanisms
Furthering the advancement of research into prions and neurodegenerative diseases
We initiate a [PSI+] response in S. cerevisiae using a plasmid that will overexpress Sup35-NM.
We insert a premature stop codon into an N-terminal CFP tag that will be read through and fluoresce during a [PSI+] response
We control read through rates by choosing the location of the premature stop codon, and can therefore control protein production in [PSI+]. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough.
ABSTRACT
Prions, or “zombie proteins,” are infectious agents that lead to a variety of neurodegenerative disorders (NDDs). They sicken cells by aggregating with each other and prevent proper protein folding leading to cell death from the accumulated damage. We propose a synthetic biology approach to better study prion propagation in the model organism S. cerevisiae. Our system involves inserting a premature stop codon into a protein open reading frame of interest or into dCas9 to respectively overexpress or knock-down protein levels during a [PSI+] response. We use Hsp104, a chaperone protein in S. cerevisiae, to demonstrate that our set-up phenotypically responds to the stop codon readthrough. This research is useful for continuously observing a phenotypic output during prion propagation in yeast and may have implications for helping to identify protein targets for both prevention and treatment of NDDs in the future.